2PBJ
GSH-heme bound microsomal prostaglandin E synthase
Functional Information from GO Data
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL A 475 |
| Chain | Residue |
| A | ARG137 |
| A | ARG146 |
| D | TYR287 |
| site_id | AC2 |
| Number of Residues | 13 |
| Details | BINDING SITE FOR RESIDUE HEM A 476 |
| Chain | Residue |
| A | SER247 |
| A | ILE264 |
| A | LEU293 |
| A | GSH477 |
| A | HOH497 |
| A | HOH514 |
| B | HOH502 |
| A | THR109 |
| A | PRO111 |
| A | PHE112 |
| A | PRO134 |
| A | VAL243 |
| A | HIS244 |
| site_id | AC3 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GSH A 477 |
| Chain | Residue |
| A | TYR107 |
| A | CYS110 |
| A | PHE112 |
| A | ARG146 |
| A | LYS147 |
| A | VAL148 |
| A | PRO149 |
| A | ASP164 |
| A | SER165 |
| A | HEM476 |
| A | HOH481 |
| A | HOH486 |
| site_id | AC4 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL B 475 |
| Chain | Residue |
| B | ARG137 |
| B | ARG146 |
| C | TYR287 |
| site_id | AC5 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM B 476 |
| Chain | Residue |
| B | THR109 |
| B | PRO111 |
| B | PHE112 |
| B | PRO134 |
| B | VAL243 |
| B | HIS244 |
| B | SER247 |
| B | ILE264 |
| B | LEU293 |
| B | GSH477 |
| B | HOH499 |
| B | HOH510 |
| site_id | AC6 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE GSH B 477 |
| Chain | Residue |
| B | TYR107 |
| B | CYS110 |
| B | PHE112 |
| B | ARG146 |
| B | LYS147 |
| B | VAL148 |
| B | PRO149 |
| B | ASP164 |
| B | SER165 |
| B | HEM476 |
| B | HOH480 |
| B | HOH485 |
| site_id | AC7 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL C 475 |
| Chain | Residue |
| B | TYR287 |
| C | ARG137 |
| C | ARG146 |
| site_id | AC8 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM C 476 |
| Chain | Residue |
| C | THR109 |
| C | CYS110 |
| C | PRO111 |
| C | PHE112 |
| C | PRO134 |
| C | VAL243 |
| C | HIS244 |
| C | SER247 |
| C | ILE264 |
| C | LEU293 |
| C | GSH477 |
| C | HOH514 |
| site_id | AC9 |
| Number of Residues | 11 |
| Details | BINDING SITE FOR RESIDUE GSH C 477 |
| Chain | Residue |
| C | TYR107 |
| C | CYS110 |
| C | PHE112 |
| C | ARG146 |
| C | LYS147 |
| C | VAL148 |
| C | ASP164 |
| C | SER165 |
| C | HEM476 |
| C | HOH484 |
| C | HOH502 |
| site_id | BC1 |
| Number of Residues | 3 |
| Details | BINDING SITE FOR RESIDUE CL D 475 |
| Chain | Residue |
| A | TYR287 |
| D | ARG137 |
| D | ARG146 |
| site_id | BC2 |
| Number of Residues | 12 |
| Details | BINDING SITE FOR RESIDUE HEM D 476 |
| Chain | Residue |
| D | THR109 |
| D | CYS110 |
| D | PRO111 |
| D | PHE112 |
| D | PRO134 |
| D | VAL243 |
| D | HIS244 |
| D | SER247 |
| D | ILE264 |
| D | LEU293 |
| D | GSH477 |
| D | HOH492 |
| site_id | BC3 |
| Number of Residues | 9 |
| Details | BINDING SITE FOR RESIDUE GSH D 477 |
| Chain | Residue |
| D | ARG146 |
| D | LYS147 |
| D | VAL148 |
| D | ASP164 |
| D | SER165 |
| D | HEM476 |
| D | TYR107 |
| D | CYS110 |
| D | PHE112 |
Functional Information from PROSITE/UniProt
| site_id | PS00195 |
| Number of Residues | 17 |
| Details | GLUTAREDOXIN_1 Glutaredoxin active site. LYqyktCPFCskVrafL |
| Chain | Residue | Details |
| A | LEU104-LEU120 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 8 |
| Details | Binding site: {"evidences":[{"source":"PubMed","id":"17585783","evidenceCode":"ECO:0000269"}]} |
| Chain | Residue | Details |
Catalytic Information from CSA
| site_id | MCSA1 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| A | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| A | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| A | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| A | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| site_id | MCSA2 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| B | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| B | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| B | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| B | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| site_id | MCSA3 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| C | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| C | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| C | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| C | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
| site_id | MCSA4 |
| Number of Residues | 4 |
| Details | M-CSA 192 |
| Chain | Residue | Details |
| D | TYR107 | activator, electrostatic stabiliser, hydrogen bond donor |
| D | CYS110 | hydrogen bond acceptor, hydrogen bond donor, nucleofuge, nucleophile, proton acceptor, proton donor |
| D | PHE112 | electrostatic stabiliser, hydrogen bond donor |
| D | CYS113 | electrostatic stabiliser, hydrogen bond acceptor, hydrogen bond donor, increase acidity |
